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The antibody against PKA C-alpha (PRKACA) was raised in Rabbit using a synthetic peptide corresponding to a sequence within amino acids 1-351 of human PKA C-alpha (PRKACA) (NP_002721.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
The antibody against PKA C-alpha (PRKACA) was raised in Rabbit using a synthetic peptide corresponding to a sequence within amino acids 1-351 of human PKA C-alpha (PRKACA) (NP_002721.1) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
| Cat.No | ADA-10375A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PKA C-alpha (PRKACA) |
| Target Synonyms | CAFD1; PKACA; PPNAD4; PKA C-alpha (PRKACA) | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.05% proclin300, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Mouse heart, Rat heart, Mouse brain, PC-12 | Application | ELISA, WB |
| Immunogen Description | A synthetic peptide corresponding to a sequence within amino acids 1-351 of human PKA C-alpha (PRKACA) (NP_002721.1). | Target Species | Human |
|---|---|---|---|
| Uniprot ID | P17612 | Immunogen Sequence |
Uniprot Id
P17612
Target Species
Human
Target Name
PRKACA
Target Full Name
cAMP-dependent protein kinase catalytic subunit alpha
Target Function
Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in chondrogenesis by mediating phosphorylation of SOX9. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock.; Phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation.
Target Involvement
Primary pigmented nodular adrenocortical disease 4 (PPNAD4)
Target Subcellular Location
Cytoplasm. Cell membrane. Nucleus. Mitochondrion. Membrane; Lipid-anchor.; [Isoform 2]: Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome.
Target Protein Families
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily
Target Tissue Specificity
Isoform 1 is ubiquitous. Isoform 2 is sperm-specific and is enriched in pachytene spermatocytes but is not detected in round spermatids.
Target Research Area
Cancer
Target Synonyms
cAMP dependent protein kinase alpha catalytic subunit; cAMP dependent protein kinase beta catalytic subunit; cAMP dependent protein kinase catalytic beta subunit isoform 4ab; cAMP dependent protein kinase catalytic subunit alpha; cAMP dependent protein kinase catalytic subunit alpha, isoform 1; cAMP dependent protein kinase catalytic subunit beta; cAMP-dependent protein kinase catalytic subunit alpha; KAPCA_HUMAN; PKA C alpha ; PKA C beta; PKA C-alpha; PKACA; PKACB; PPNAD4; PRKACA; PRKACAA; PRKACB ; Protein kinase A catalytic subunit alpha; Protein kinase A catalytic subunit; Protein kinase A catalytic subunit beta; Protein kinase, cAMP dependent, catalytic, alpha; Protein kinase, cAMP dependent, catalytic, beta
Target Background
This gene encodes one of the catalytic subunits of protein kinase A, which exists as a tetrameric holoenzyme with two regulatory subunits and two catalytic subunits, in its inactive form. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. cAMP-dependent phosphorylation of proteins by protein kinase A is important to many cellular processes, including differentiation, proliferation, and apoptosis. Constitutive activation of this gene caused either by somatic mutations, or genomic duplications of regions that include this gene, have been associated with hyperplasias and adenomas of the adrenal cortex and are linked to corticotropin-independent Cushing's syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms. Tissue-specific isoforms that differ at the N-terminus have been described, and these isoforms may differ in the post-translational modifications that occur at the N-terminus of some isoforms.
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